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Database: UniProt
Entry: A0A0F5VC46_9GAMM
LinkDB: A0A0F5VC46_9GAMM
Original site: A0A0F5VC46_9GAMM 
ID   A0A0F5VC46_9GAMM        Unreviewed;       571 AA.
AC   A0A0F5VC46;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   27-MAR-2024, entry version 38.
DE   RecName: Full=Sensor protein {ECO:0000256|PIRNR:PIRNR003167};
DE            EC=2.7.13.3 {ECO:0000256|PIRNR:PIRNR003167};
GN   ORFNames=KY46_15130 {ECO:0000313|EMBL:KKC99039.1};
OS   Photobacterium halotolerans.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Photobacterium.
OX   NCBI_TaxID=265726 {ECO:0000313|EMBL:KKC99039.1, ECO:0000313|Proteomes:UP000033633};
RN   [1] {ECO:0000313|EMBL:KKC99039.1, ECO:0000313|Proteomes:UP000033633}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MELD1 {ECO:0000313|EMBL:KKC99039.1,
RC   ECO:0000313|Proteomes:UP000033633};
RA   Mathew D.C., Huang C.-C.;
RT   "Mercury Reductase activity and rhizosphere competence traits in the genome
RT   of root associated Photobacterium halotolerans MELD1.";
RL   Submitted (DEC-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L-
CC         histidine.; EC=2.7.13.3; Evidence={ECO:0000256|ARBA:ARBA00000085,
CC         ECO:0000256|PIRNR:PIRNR003167};
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane
CC       {ECO:0000256|ARBA:ARBA00004429}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004429}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004141}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KKC99039.1}.
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DR   EMBL; JWYV01000014; KKC99039.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0F5VC46; -.
DR   STRING; 265726.KY46_15130; -.
DR   PATRIC; fig|265726.11.peg.1288; -.
DR   Proteomes; UP000033633; Unassembled WGS sequence.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0046983; F:protein dimerization activity; IEA:UniProtKB-UniRule.
DR   CDD; cd06225; HAMP; 1.
DR   CDD; cd16917; HATPase_UhpB-NarQ-NarX-like; 1.
DR   CDD; cd22899; NarQ_sensor; 1.
DR   Gene3D; 1.20.5.1930; -; 1.
DR   Gene3D; 6.10.340.10; -; 1.
DR   Gene3D; 1.20.120.960; Histidine kinase NarX, sensor domain; 1.
DR   Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR   InterPro; IPR003660; HAMP_dom.
DR   InterPro; IPR003594; HATPase_C.
DR   InterPro; IPR036890; HATPase_C_sf.
DR   InterPro; IPR005467; His_kinase_dom.
DR   InterPro; IPR029095; NarX-like_N.
DR   InterPro; IPR042295; NarX-like_N_sf.
DR   InterPro; IPR016380; Sig_transdc_His_kin_NarX/NarQ.
DR   InterPro; IPR011712; Sig_transdc_His_kin_sub3_dim/P.
DR   PANTHER; PTHR24421; NITRATE/NITRITE SENSOR PROTEIN NARX-RELATED; 1.
DR   PANTHER; PTHR24421:SF66; NITRATE_NITRITE SENSOR PROTEIN NARQ; 1.
DR   Pfam; PF00672; HAMP; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF07730; HisKA_3; 1.
DR   Pfam; PF13675; PilJ; 1.
DR   PIRSF; PIRSF003167; STHK_NarX/NarQ; 1.
DR   SMART; SM00304; HAMP; 1.
DR   SMART; SM00387; HATPase_c; 1.
DR   SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR   SUPFAM; SSF158472; HAMP domain-like; 1.
DR   PROSITE; PS50885; HAMP; 1.
DR   PROSITE; PS50109; HIS_KIN; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|PIRNR:PIRNR003167};
KW   Cell inner membrane {ECO:0000256|PIRNR:PIRNR003167};
KW   Cell membrane {ECO:0000256|PIRNR:PIRNR003167};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|PIRNR:PIRNR003167};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|PIRNR:PIRNR003167};
KW   Nucleotide-binding {ECO:0000256|PIRNR:PIRNR003167};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000033633};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR003167};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius};
KW   Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012,
KW   ECO:0000256|PIRNR:PIRNR003167}.
FT   TRANSMEM        6..28
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        153..173
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          178..230
FT                   /note="HAMP"
FT                   /evidence="ECO:0000259|PROSITE:PS50885"
FT   DOMAIN          371..565
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
SQ   SEQUENCE   571 AA;  63565 MW;  A328EB1C1CDA548D CRC64;
     MPKSGLLAGS VTGTVARVML AIVLLSLLTT GATMFAVNAS RYDAEVVNLA GSLRMQSYRL
     AFQLAEQGEA NAQDIAQFSQ TLATPAMTSL LGLTTPRELT QSYQAILDDW QRLSALLTDQ
     PPDYFIRQVP EFVDRIDHFV YELQAFSKQK LQMMAIIAGL GLGLILLLAL FAIQYSRRFI
     VPPLHNLLIA SQQVQSRNFA VRVQEDSQNE LGTLARAFNQ MAEELGQSYQ ALEHTVEEKT
     HRLQEANNAL KTLYDCAQLL SMNRIQAKHF SQVLGRLMQL EGFAAIRLVV EEGQGIRTEF
     QAGKPDENQS WHHHALKQEA QHLGTLWWQH TLPCPDPAMI ISVGHLLSRA LHAHQIQVQN
     EQLLLMEERA TIARELHDSL AQALSYLKIQ LTLLKRQLAT SPESANGVID DIDQGLSQAY
     RQLRELLNTF RLSVKPGKLG DALNDMLNGL RNQTNASILL HNQLPSIQLT AQQQIHLLHL
     TREAVINAIK HARAQTITVE CVQQENHVLV NIADDGQGFN PDHSKTAHYG LTIMNERAES
     LGGQLTITSA PGEGCQIQLK FALQNTGNNH E
//
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